Search Results - "Dyson, H"
-
1
NMR illuminates intrinsic disorder
Published in Current opinion in structural biology (01-10-2021)“…Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of intrinsically disordered proteins (IDPs) and intrinsically disordered…”
Get full text
Journal Article -
2
Making Sense of Intrinsically Disordered Proteins
Published in Biophysical journal (08-03-2016)“…Proteins form the molecular scaffolding of life and are essential to catalyzing the chemical reactions that sustain living systems. These characteristics have…”
Get full text
Journal Article -
3
Vital for Viruses: Intrinsically Disordered Proteins
Published in Journal of molecular biology (01-06-2023)“…[Display omitted] •The minimal genetic material of viruses must be used with the utmost efficiency.•One efficient tactic is to use IDPs to hijack cellular…”
Get full text
Journal Article -
4
Intrinsically disordered proteins in cellular signalling and regulation
Published in Nature reviews. Molecular cell biology (01-01-2015)“…Key Points Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins that may also contain structured domains mediate…”
Get full text
Journal Article -
5
Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300
Published in The Journal of biological chemistry (25-03-2016)“…The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered…”
Get full text
Journal Article -
6
Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain
Published in Proceedings of the National Academy of Sciences - PNAS (27-11-2018)“…Atomic resolution characterization of the full-length p53 tetramer has been hampered by its size and the presence of extensive intrinsically disordered regions…”
Get full text
Journal Article -
7
-
8
Early Strides in NMR Dynamics Measurements
Published in Biochemistry (Easton) (23-11-2021)“…The study of protein dynamics using the measurement of relaxation times by NMR was based on a set of studies in the mid-20th century that outlined theories and…”
Get full text
Journal Article -
9
More pandemic reflections
Published in Biophysical journal (16-11-2021)Get full text
Journal Article -
10
Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding
Published in Proceedings of the National Academy of Sciences - PNAS (04-08-2015)“…Intrinsically disordered proteins (IDPs) frequently function in protein interaction networks that regulate crucial cellular signaling pathways. Many IDPs…”
Get full text
Journal Article -
11
Hypersensitive termination of the hypoxic response by a disordered protein switch
Published in Nature (London) (16-03-2017)“…The intrinsically disordered CITED2 negative feedback regulator displaces the tightly bound hypoxia-inducible transcription factor HIF-1α from their common…”
Get full text
Journal Article -
12
Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation
Published in Journal of molecular biology (03-08-2018)“…Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally…”
Get full text
Journal Article -
13
Diversity at BJ: The editors, the reviewers, the authors
Published in Biophysical journal (20-04-2021)Get full text
Journal Article -
14
Linking folding and binding
Published in Current opinion in structural biology (01-02-2009)“…Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years…”
Get full text
Journal Article -
15
Reflections on the Pandemic
Published in Biophysical journal (01-09-2020)Get full text
Journal Article -
16
Functional advantages of dynamic protein disorder
Published in FEBS letters (14-09-2015)“…Intrinsically disordered proteins participate in many important cellular regulatory processes. The absence of a well-defined structure in the free state of a…”
Get full text
Journal Article -
17
A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA binding
Published in Proceedings of the National Academy of Sciences - PNAS (05-01-2021)“…The tumor-suppressor p53 is a critical regulator of the cellular response to DNA damage and is tightly regulated by posttranslational modifications. Thr55 in…”
Get full text
Journal Article -
18
Kinetic analysis of the multistep aggregation pathway of human transthyretin
Published in Proceedings of the National Academy of Sciences - PNAS (03-07-2018)“…Aggregation of transthyretin (TTR) is the causative agent for TTR cardiomyopathy and polyneuropathy amyloidoses. Aggregation is initiated by dissociation of…”
Get full text
Journal Article -
19
Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins
Published in Journal of biomolecular NMR (01-12-2019)“…The 2019 ISMAR Prize recognized NMR studies of disordered proteins. Here we provide a highly personal perspective on the discovery of intrinsically disordered…”
Get full text
Journal Article -
20
Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins
Published in Proceedings of the National Academy of Sciences - PNAS (18-01-2022)“…Intrinsically disordered proteins must compete for binding to common regulatory targets to carry out their biological functions. Previously, we showed that the…”
Get full text
Journal Article